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. Author manuscript; available in PMC: 2008 Sep 26.
Published in final edited form as: J Biol Chem. 2003 Jul 16;278(41):39269–39279. doi: 10.1074/jbc.M305830200

Fig. 2. pMJK-1-driven overexpression of 1-phosphatase in membranes of R. etli CE3.

Fig. 2

The 1-phosphatase activity present in membranes of R. etli CE3/pMJK-1 was compared with that of membranes from R. etli CE3 harboring the vector pLAFR-1. The reactions (typically 20 μl) were carried out at 30 °C with 5 μM Kdo2-[4′-32P]lipid IVA as the substrate. Product formation was detected by TLC and PhosphorImager analysis.